Evidence map›Paper›PMID 23684952›Full record

ReviewBiochimica et biophysica acta2014

Ubiquitin-independent proteasomal degradation.

Jenny Erales, Philip Coffino

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 125 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
125citing papers in PubMed, 1 pooled it
7.5field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

125 citing papers in PubMed, 1 synthesis or guideline pooled it, 243 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Identification of a Ubiquitin-Independent Degron by a Reporter Assay.Methods in molecular biology (Clifton, N.J.) · 2026
    Article
  8. Structure of the TXNL1-bound proteasome.Nature structural & molecular biology · 2025
    Article
  9. Article
  10. Review
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Ubiquitin-Independent Degradation: An Emerging PROTAC Approach?BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  19. Article
  20. Article

65 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Jenny EralesDepartment of Microbiology & Immunology, University of California, San Francisco, San Francisco, CA 94127, USA.
Philip Coffino
University of California, San Francisco · US

Funding

Ubiquitin-Independent Proteasome DegradationR01GM045335 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI COFFINO, PHILIP · 1991 to 2012
$4.5M
NIGMS NIH HHS GM45335NIGMS NIH HHS R01 GM045335
6 · The paper itself

Abstract

Most proteasome substrates are marked for degradation by ubiquitin conjugation, but some are targeted by other means. The properties of these exceptional cases provide insights into the general requirements for proteasomal degradation. Here the focus is on three ubiquitin-independent substrates that have been the subject of detailed study. These are Rpn4, a transcriptional regulator of proteasome homeostasis, thymidylate synthase, an enzyme required for production of DNA precursors and ornithine decarboxylase, the initial enzyme committed to polyamine biosynthesis. It can be inferred from these cases that proteasome association and the presence of an unstructured region are the sole prerequisites for degradation. Based on that inference, artificial substrates have been designed to test the proteasome's capacity for substrate processing and its limitations. Ubiquitin-independent substrates may in some cases be a remnant of the pre-ubiquitome world, but in other cases could provide optimized regulatory solutions. This article is part of a Special Issue entitled: Ubiquitin-Proteasome System. Guest Editors: Thomas Sommer and Dieter H. Wolf.

Indexed as

ProteolysisAnimalsDNA-Binding ProteinsHumansOrnithine DecarboxylaseProteasome Endopeptidase ComplexProtein Structure, TertiaryProtein UnfoldingSaccharomyces cerevisiae ProteinsThymidylate SynthaseTranscription FactorsUbiquitinDNA-Binding ProteinsOrnithine DecarboxylaseProteasome Endopeptidase ComplexRPN4 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsThymidylate SynthaseTranscription FactorsUbiquitinDegradationDegronIntrinsically disordered proteinsOrnithine decarboxylaseProteasomeProtein disorderRpn4Thymidylate synthaseUbiquitin

Identifiers

PMID23684952
PMCPMC3770795
OpenAlexW2001803273

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.